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Crystal strcuture of amidohydrolase from pseudomonas aeruginosa

Analyse Crystal strcuture of amidohydrolase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2I5G
Type
protein
Length
650 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Amidohydrolase
UniProt
Q9HTG8
Pockets
3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAmidohydrolaseprotein32545% helix, 16% strandQ9HTG8

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11370.470.7817empty
21330.460.7716empty
3740.380.7918empty

Interfaces

1 interface between chains.

  • A–B · 1087 Ų buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 2I5G · Crystal strcuture of amidohydrolase from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00

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